Chilling stress suppresses chloroplast development and nuclear gene expression in leaves of mung bean seedlings

被引:40
作者
Yang, MT
Chen, SL
Lin, CY
Chen, YM
机构
[1] Natl Taiwan Univ, Inst Plant Biol, Taipei 106, Taiwan
[2] Ming Chuan Univ, Dept Biotechnol, Taoyuan 333, Taiwan
关键词
chilling stress; chilling-sensitive plants; chloroplast development; cold-suppressed genes; etioplast;
D O I
10.1007/s00425-004-1451-y
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Etiolated leaves of 28 degrees C-dark-grown mung bean (Vigna radiata L. cv. 2937) seedlings fail to turn green after being shifted to a light and cold environment. At the visible phenotypic level, incapability of leaf greening is the only failure event for the de-etiolation of mung bean seedlings at low temperature. Ultrastructural studies revealed that chloroplast development was completely suppressed by chilling treatment. A cDNA library originating from 28 degrees C-light-grown seedling leaves was constructed for screening cold-suppressed (cos) genes. Thirteen full-length cDNA clones were obtained, with 12 clones encoding chloroplast proteins, which, according to their known physiological functions, were important for chloroplast development and photosynthesis. Another cos cDNA encodes CYP90A2, which is a cytochrome P450 protein involved in the biosynthesis of brassinosteroid hormones. All cos genes are light-regulated at normal temperature. The influence of chilling stress on cos expression was examined in 10 degrees C-light- and 10 degrees C-dark-grown etiolated seedlings, and in 10 degrees C-light-grown green plants. The data show that cos expression in these three treatments is severely suppressed. This suppression is controlled at the transcriptional level, as demonstrated by nuclear runoff experiments, and is reversible because cos mRNAs accumulate again after the cold-treated plants have been transferred to 28 degrees C.
引用
收藏
页码:374 / 385
页数:12
相关论文
共 60 条
[1]  
AGUAN K, 1993, MOL GEN GENET, V24, P1
[2]   PROTEIN-PHOSPHORYLATION IN REGULATION OF PHOTOSYNTHESIS [J].
ALLEN, JF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1098 (03) :275-335
[3]  
Anderson SL, 1997, PLANT CELL, V9, P1727, DOI 10.1105/tpc.9.10.1727
[4]  
APEL K, 1980, EUR J BIOCHEM, V111, P251, DOI 10.1111/j.1432-1033.1980.tb06100.x
[5]   IDENTIFICATION OF NADPH-PROTOCHLOROPHYLLIDE OXIDOREDUCTASE-A AND OXIDOREDUCTASE-B - A BRANCHED PATHWAY FOR LIGHT-DEPENDENT CHLOROPHYLL BIOSYNTHESIS IN ARABIDOPSIS-THALIANA [J].
ARMSTRONG, GA ;
RUNGE, S ;
FRICK, G ;
SPERLING, U ;
APEL, K .
PLANT PHYSIOLOGY, 1995, 108 (04) :1505-1517
[6]   PHOTOINHIBITION OF PHOTOSYSTEM-2 - INACTIVATION, PROTEIN DAMAGE AND TURNOVER [J].
ARO, EM ;
VIRGIN, I ;
ANDERSSON, B .
BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1143 (02) :113-134
[7]  
Ausubel F.M., 1994, CURRENT PROTOCOLS MO
[8]   THE ROLE OF CARBONIC-ANHYDRASE IN PHOTOSYNTHESIS [J].
BADGER, MR ;
PRICE, GD .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1994, 45 :369-392
[9]   Regulation of transcript levels of the Arabidopsis cytochrome P450 genes involved in brassinosteroid biosynthesis [J].
Bancos, S ;
Nomura, T ;
Sato, T ;
Molnár, G ;
Bishop, GJ ;
Koncz, C ;
Yokota, T ;
Nagy, F ;
Szekeres, M .
PLANT PHYSIOLOGY, 2002, 130 (01) :504-513
[10]   SPECIFICITY OF OLIGO (DT)-CELLULOSE CHROMATOGRAPHY IN ISOLATION OF POLYADENYLATED RNA [J].
BANTLE, JA ;
MAXWELL, IH ;
HAHN, WE .
ANALYTICAL BIOCHEMISTRY, 1976, 72 (1-2) :413-427